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Volumn 345, Issue 1, 2005, Pages 29-38

X-ray structural studies of Mycobacterium tuberculosis RRF and a comparative study of RRFs of known structure. Molecular plasticity and biological implications

Author keywords

domain motion; Mycobacterium tuberculosis; protein synthesis; ribosome recycling factor; structural genomics

Indexed keywords

ARTICLE; COMPARATIVE STUDY; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; LOW TEMPERATURE; MOLECULAR INTERACTION; MYCOBACTERIUM TUBERCULOSIS; PLASTICITY; PRIORITY JOURNAL; RADIATION INJURY; RIBOSOME; ROOM TEMPERATURE; ROTATION; X RAY DIFFRACTION;

EID: 9644260557     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.10.034     Document Type: Article
Times cited : (34)

References (41)
  • 1
    • 0029950071 scopus 로고    scopus 로고
    • Ribosome recycling by ribosome recycling factor (RRF) - An important but overlooked step of protein biosynthesis
    • L. Janosi, H. Hara, S. Zhang, and A. Kaji Ribosome recycling by ribosome recycling factor (RRF) - an important but overlooked step of protein biosynthesis Advan. Biophys. 32 1996 121 201
    • (1996) Advan. Biophys. , vol.32 , pp. 121-201
    • Janosi, L.1    Hara, H.2    Zhang, S.3    Kaji, A.4
  • 2
    • 0035355353 scopus 로고    scopus 로고
    • Specific interaction between the ribosome recycling factor and the elongation factor G from Mycobacterium tuberculosis mediated peptidyl-tRNA release and ribosome recycling in Escherichia coli
    • A.R. Rao, and U. Varshney Specific interaction between the ribosome recycling factor and the elongation factor G from Mycobacterium tuberculosis mediated peptidyl-tRNA release and ribosome recycling in Escherichia coli EMBO J. 20 2001 2977 2986
    • (2001) EMBO J. , vol.20 , pp. 2977-2986
    • Rao, A.R.1    Varshney, U.2
  • 3
    • 0032481304 scopus 로고    scopus 로고
    • Evidence for in vivo ribosome recycling, the fourth step in protein biosynthesis
    • L. Janosi, S. Mottagui-Tabar, L.A. Isaksson, Y. Sekine, E. Ohtsubo, and S. Zhang Evidence for in vivo ribosome recycling, the fourth step in protein biosynthesis EMBO J. 17 1998 1141 1151
    • (1998) EMBO J. , vol.17 , pp. 1141-1151
    • Janosi, L.1    Mottagui-Tabar, S.2    Isaksson, L.A.3    Sekine, Y.4    Ohtsubo, E.5    Zhang, S.6
  • 4
    • 0028314657 scopus 로고
    • Ribosome recycling factor (ribosome releasing factor) is essential for bacterial growth
    • L. Janosi, I. Shimizu, and A. Kaji Ribosome recycling factor (ribosome releasing factor) is essential for bacterial growth Proc. Natl Acad. Sci. USA 91 1994 4249 4253
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 4249-4253
    • Janosi, L.1    Shimizu, I.2    Kaji, A.3
  • 5
    • 0032497314 scopus 로고    scopus 로고
    • Disassembly of the post-termination complex and reduction of translational error by ribosome recycling factor (RRF) - A possible new target for antibacterial agents
    • A. Kaji, E. Teyssier, and G. Hirokawa Disassembly of the post-termination complex and reduction of translational error by ribosome recycling factor (RRF) - a possible new target for antibacterial agents Biochem. Biophys. Res. Commun. 250 1998 1 4
    • (1998) Biochem. Biophys. Res. Commun. , vol.250 , pp. 1-4
    • Kaji, A.1    Teyssier, E.2    Hirokawa, G.3
  • 6
    • 0036566330 scopus 로고    scopus 로고
    • Post-termination complex disassembly by ribosome recycling factor, a functional tRNA mimic
    • G. Hirokawa, M.C. Kiel, A. Muto, M. Selmer, V.S. Raj, and A. Liljas Post-termination complex disassembly by ribosome recycling factor, a functional tRNA mimic EMBO J. 21 2002 2272 2281
    • (2002) EMBO J. , vol.21 , pp. 2272-2281
    • Hirokawa, G.1    Kiel, M.C.2    Muto, A.3    Selmer, M.4    Raj, V.S.5    Liljas, A.6
  • 7
    • 0033063428 scopus 로고    scopus 로고
    • Novel roles for classical factors at the interface between translation termination and initiation
    • R. Karimi, M.Y. Pavlov, R.H. Buckingham, and M. Ehrenberg Novel roles for classical factors at the interface between translation termination and initiation Mol. Cell 3 1999 601 609
    • (1999) Mol. Cell , vol.3 , pp. 601-609
    • Karimi, R.1    Pavlov, M.Y.2    Buckingham, R.H.3    Ehrenberg, M.4
  • 8
    • 0034679627 scopus 로고    scopus 로고
    • Role of ribosome recycling factor (RRF) in translational coupling
    • Y. Inokuchi, A. Hirashima, Y. Sekine, L. Janosi, and A. Kaji Role of ribosome recycling factor (RRF) in translational coupling EMBO J. 19 2000 3788 3798
    • (2000) EMBO J. , vol.19 , pp. 3788-3798
    • Inokuchi, Y.1    Hirashima, A.2    Sekine, Y.3    Janosi, L.4    Kaji, A.5
  • 9
    • 0033579365 scopus 로고    scopus 로고
    • Crystal structure of Thermotoga maritima ribosome recycling factor: A tRNA mimic
    • M. Selmer, S. Al-Karadaghi, G. Hirokawa, A. Kaji, and A. Liljas Crystal structure of Thermotoga maritima ribosome recycling factor: a tRNA mimic Science 286 1999 2349 2352
    • (1999) Science , vol.286 , pp. 2349-2352
    • Selmer, M.1    Al-Karadaghi, S.2    Hirokawa, G.3    Kaji, A.4    Liljas, A.5
  • 10
    • 0343618468 scopus 로고    scopus 로고
    • Crystal structure of the ribosome recycling factor from Escherichia coli
    • K.K. Kim, K. Min, and S.W. Suh Crystal structure of the ribosome recycling factor from Escherichia coli EMBO J. 19 2000 2362 2370
    • (2000) EMBO J. , vol.19 , pp. 2362-2370
    • Kim, K.K.1    Min, K.2    Suh, S.W.3
  • 11
    • 0033751564 scopus 로고    scopus 로고
    • Crystal structure combined with genetic analysis of the Thermus thermophilus ribosome recycling factor shows that a flexible hinge may act as a functional switch
    • T. Toyoda, Q.F. Tin, K. Ito, T. Fujiwara, T. Kumasaka, and M. Yamamoto Crystal structure combined with genetic analysis of the Thermus thermophilus ribosome recycling factor shows that a flexible hinge may act as a functional switch RNA 6 2000 1432 1444
    • (2000) RNA , vol.6 , pp. 1432-1444
    • Toyoda, T.1    Tin, Q.F.2    Ito, K.3    Fujiwara, T.4    Kumasaka, T.5    Yamamoto, M.6
  • 13
    • 0036006790 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic studies of a mutant of ribosome recycling factor from Escherichia coli, Arg132Gly
    • H. Nakano, S. Uchiyama, T. Yoshida, T. Ohkubo, H. Kato, Y. Yamagata, and Y. Kobayashi Crystallization and preliminary X-ray crystallographic studies of a mutant of ribosome recycling factor from Escherichia coli, Arg132Gly Acta Crystallog. sect. D 58 2002 124 126
    • (2002) Acta Crystallog. Sect. D , vol.58 , pp. 124-126
    • Nakano, H.1    Uchiyama, S.2    Yoshida, T.3    Ohkubo, T.4    Kato, H.5    Yamagata, Y.6    Kobayashi, Y.7
  • 14
    • 0037474260 scopus 로고    scopus 로고
    • Structure and binding mode of a ribosome recycling factor (RRF) from mesophilic bacterium
    • H. Nakano, T. Yoshida, S. Uchiyama, M. Kawachi, H. Matsuo, and T. Kato Structure and binding mode of a ribosome recycling factor (RRF) from mesophilic bacterium J. Biol. Chem. 278 2003 3427 3436
    • (2003) J. Biol. Chem. , vol.278 , pp. 3427-3436
    • Nakano, H.1    Yoshida, T.2    Uchiyama, S.3    Kawachi, M.4    Matsuo, H.5    Kato, T.6
  • 15
    • 0037020031 scopus 로고    scopus 로고
    • Orientation of ribosome recycling factor in the ribosome from directed hydroxyl radical probing
    • L. Lancaster, M.C. Kiel, A. Kaji, and H.F. Noller Orientation of ribosome recycling factor in the ribosome from directed hydroxyl radical probing Cell 111 2002 129 140
    • (2002) Cell , vol.111 , pp. 129-140
    • Lancaster, L.1    Kiel, M.C.2    Kaji, A.3    Noller, H.F.4
  • 17
    • 2942643924 scopus 로고    scopus 로고
    • Visualization of ribosome-recycling factor on the Escherichia coli 70S ribosome: Functional implications
    • R.K. Agrawal, M.R. Sharma, M.C. Kiel, G. Hirokawa, T.M. Booth, and C.M. Spahn Visualization of ribosome-recycling factor on the Escherichia coli 70S ribosome: functional implications Proc. Natl Acad. Sci. USA 101 2004 8900 8905
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 8900-8905
    • Agrawal, R.K.1    Sharma, M.R.2    Kiel, M.C.3    Hirokawa, G.4    Booth, T.M.5    Spahn, C.M.6
  • 18
    • 0036296507 scopus 로고    scopus 로고
    • Elongation factor G participates in ribosome recycling disassembly by interacting with ribosome recycling factor at their tRNA-mimicry domains
    • K. Ito, T. Fujiwara, T. Toyoda, and Y. Nakamura Elongation factor G participates in ribosome recycling disassembly by interacting with ribosome recycling factor at their tRNA-mimicry domains Mol. Cell 9 2002 1263 1272
    • (2002) Mol. Cell , vol.9 , pp. 1263-1272
    • Ito, K.1    Fujiwara, T.2    Toyoda, T.3    Nakamura, Y.4
  • 19
    • 0036953086 scopus 로고    scopus 로고
    • Characterisation of Mycobacterium tuberculosis ribosome recycling factor (RRF) and a mutant lacking six amino acids from the C-terminal end reveals that the C-terminal residues are important for its occupancy on the ribosome
    • A.R. Rao, and U. Varshney Characterisation of Mycobacterium tuberculosis ribosome recycling factor (RRF) and a mutant lacking six amino acids from the C-terminal end reveals that the C-terminal residues are important for its occupancy on the ribosome Microbiology 148 2002 3913 3920
    • (2002) Microbiology , vol.148 , pp. 3913-3920
    • Rao, A.R.1    Varshney, U.2
  • 20
    • 0033009527 scopus 로고    scopus 로고
    • Amber mutations in ribosome recycling factors of Escherichia coli and Thermus thermophilus: Evidence for C-terminal modulator element
    • T. Fujiwara, K. Ito, T. Nakayashiki, and Y. Nakamura Amber mutations in ribosome recycling factors of Escherichia coli and Thermus thermophilus: evidence for C-terminal modulator element FEBS Letters 447 1999 297 302
    • (1999) FEBS Letters , vol.447 , pp. 297-302
    • Fujiwara, T.1    Ito, K.2    Nakayashiki, T.3    Nakamura, Y.4
  • 22
    • 0036850805 scopus 로고    scopus 로고
    • Physical and chemical considerations of damage induced in protein crystals by synchrotron radiation: A radiation chemical perspective
    • P. O'Neill, D.L. Stevens, and E.F. Garman Physical and chemical considerations of damage induced in protein crystals by synchrotron radiation: a radiation chemical perspective J. Synchrotron Rad. 9 2002 329 332
    • (2002) J. Synchrotron Rad. , vol.9 , pp. 329-332
    • O'Neill, P.1    Stevens, D.L.2    Garman, E.F.3
  • 23
    • 0034055545 scopus 로고    scopus 로고
    • Structural changes in a cryo-cooled protein crystal owing to radiation damage
    • W.P. Burmeister Structural changes in a cryo-cooled protein crystal owing to radiation damage Acta Crystallog. sect. D 56 2000 328 341
    • (2000) Acta Crystallog. Sect. D , vol.56 , pp. 328-341
    • Burmeister, W.P.1
  • 25
    • 3042582299 scopus 로고    scopus 로고
    • X-ray analysis of Mycobacterium smegmatis Dps and a comparative study involving other Dps and Dps-like molecules
    • S. Roy, S. Gupta, S. Das, K. Sekar, D. Chatterji, and M. Vijayan X-ray analysis of Mycobacterium smegmatis Dps and a comparative study involving other Dps and Dps-like molecules J. Mol. Biol. 339 2004 1103 1113
    • (2004) J. Mol. Biol. , vol.339 , pp. 1103-1113
    • Roy, S.1    Gupta, S.2    Das, S.3    Sekar, K.4    Chatterji, D.5    Vijayan, M.6
  • 26
    • 0036008503 scopus 로고    scopus 로고
    • A genetic algorithm for the identification of conformationally invariant regions in protein molecules
    • T.R. Schneider A genetic algorithm for the identification of conformationally invariant regions in protein molecules Acta Crystallog. sect. D 58 2002 195 208
    • (2002) Acta Crystallog. Sect. D , vol.58 , pp. 195-208
    • Schneider, T.R.1
  • 28
    • 0034487341 scopus 로고    scopus 로고
    • Interaction of ribosome recycling factor and elongation factor EF-G with E. coli ribosomes studied by the surface plasmon resonance technique
    • T. Ishino, K. Atarashi, S. Uchiyama, T. Yamami, Y. Saihara, and T. Yoshida Interaction of ribosome recycling factor and elongation factor EF-G with E. coli ribosomes studied by the surface plasmon resonance technique Genes Cells 5 2000 953 963
    • (2000) Genes Cells , vol.5 , pp. 953-963
    • Ishino, T.1    Atarashi, K.2    Uchiyama, S.3    Yamami, T.4    Saihara, Y.5    Yoshida, T.6
  • 29
    • 0033758853 scopus 로고    scopus 로고
    • Inhibitory effect of heterologous ribosome recycling factor on growth of Escherichia coli
    • K. Atarashi, and A. Kaji Inhibitory effect of heterologous ribosome recycling factor on growth of Escherichia coli J. Bacteriol. 182 2000 6154 6160
    • (2000) J. Bacteriol. , vol.182 , pp. 6154-6160
    • Atarashi, K.1    Kaji, A.2
  • 30
    • 0242286001 scopus 로고    scopus 로고
    • Temperature-sensitive mutation in yeast mitochondrial ribosome recycling factor (RRF)
    • E. Teyssier, G. Hirokawa, A. Tretiakova, B. Jameson, A. Kaji, and H. Kaji Temperature-sensitive mutation in yeast mitochondrial ribosome recycling factor (RRF) Nucl. Acids Res. 31 2003 4218 4226
    • (2003) Nucl. Acids Res. , vol.31 , pp. 4218-4226
    • Teyssier, E.1    Hirokawa, G.2    Tretiakova, A.3    Jameson, B.4    Kaji, A.5    Kaji, H.6
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 32
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallog. sect. D 50 1994 760 763
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 33
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • J. Navaza AMoRe: an automated package for molecular replacement Acta Crystallog. sect. A 50 1994 157 163
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 35
    • 0000356656 scopus 로고
    • A graphic model building and refinement system for macromolecules
    • T.A. Jones A graphic model building and refinement system for macromolecules J. Appl. Crytsallog. 11 1971 268 272
    • (1971) J. Appl. Crytsallog. , vol.11 , pp. 268-272
    • Jones, T.A.1
  • 36
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS refinement in REFMAC at moderate resolutions
    • M.D. Winn, G.N. Murshdov, and M.Z. Papiz Macromolecular TLS refinement in REFMAC at moderate resolutions Methods Enzymol. 374 2003 300 321
    • (2003) Methods Enzymol. , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshdov, G.N.2    Papiz, M.Z.3
  • 37
    • 0001679473 scopus 로고    scopus 로고
    • ALIGN: A program to superimpose protein coordinates, accounting for insertions and deletions
    • G.E. Cohen ALIGN: a program to superimpose protein coordinates, accounting for insertions and deletions J. Appl. Crystallog. 30 1997 1160 1161
    • (1997) J. Appl. Crystallog. , vol.30 , pp. 1160-1161
    • Cohen, G.E.1
  • 39
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • R.M. Esnouf An extensively modified version of MolScript that includes greatly enhanced coloring capabilities J. Mol. Graph. 15 1997 132 134
    • (1997) J. Mol. Graph. , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 40
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • S.K.A. Nicholls, and B. Honig Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons Proteins: Struct. Funct. Genet. 11 1991 282 296
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 282-296
    • Nicholls, S.K.A.1    Honig, B.2
  • 41
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereo chemical quality of protein structures
    • R.A. Laskowski, M.W. MacArthur, D.S. Moss, and J.M. Thornton PROCHECK: a program to check the stereo chemical quality of protein structures J. Appl. Crystallog. 26 1993 283 291
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4


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